Hedge P J, Spratt B G
FEBS Lett. 1984 Oct 15;176(1):179-84. doi: 10.1016/0014-5793(84)80936-9.
A gene fusion that links the COOH-terminal 349 amino acids of penicillin-binding protein 3 (60 kDa) of E. coli to the NH2-terminus of beta-galactosidase has been constructed. The fusion protein (38.5 kDa) retains the ability to bind benzylpenicillin with high affinity, establishing that the penicillin-binding domain (and presumably the penicillin-sensitive transpeptidase activity) of this high molecular mass penicillin-binding protein is located on a COOH-terminal functional domain.
构建了一种基因融合体,它将大肠杆菌青霉素结合蛋白3(60 kDa)的羧基末端349个氨基酸与β-半乳糖苷酶的氨基末端连接起来。融合蛋白(38.5 kDa)保留了以高亲和力结合苄青霉素的能力,这表明这种高分子量青霉素结合蛋白的青霉素结合结构域(以及推测的青霉素敏感转肽酶活性)位于羧基末端功能域上。